Amino acid sequence analyses of porcine heart mitochondrial malate dehydrogenase (mMDH) and Beta-hydroxyacyl CoA dehydrogenase (Beta HADH) are in progress. The CNBr fragments of succinylated mMDH have been isolated in homogeneous form and partial or complete sequence data obtained on them. Tryptic and chymotyptic peptides accounting for over two-thirds of the residues have been analyzed which provide most of the overlaps for the CNBr fragments. A nearly complete sequence of Beta HAH has been obtained. In addition to short segments, only one overlap remains to be established. Studies in the biosynthesis of the cytoplasmic and mitochondrial forms of MDH have been initiated utilizing a cell-free system. In other studies, the amino acid sequence of E. coli alkaline phosphatase is complete except for one segment of about fifteen residues. Two routes to obtain the requisite information are being developed. This information has been transmitted to the crystallographers determining the three-dimensional structure and joint analyses are planned. Only nine residues remain to be determined in the crab collagenase. Model building studies using the backbone coordinates of porcine elastase have been started. Sequence analysis of bovine spinal cord protein (SCP) have been initiated. Over half the sequence (amino terminal end) has been determined which has revealed the identity of this protein with the peripheral myelin protein P-2. Stuides on the localization of SCP to resolve apparent descrepancies between the function of P2 and SCP are in progress.